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The chromatin-modifying protein HUB2 is involved in the regulation of lignin composition in xylem vessels

PIRIN2 (PRN2) was earlier reported to suppress syringyl (S)-type lignin accumulation of xylem vessels of Arabidopsis thaliana. In the present study, we report yeast two-hybrid results supporting the interaction of PRN2 with HISTONE MONOUBIQUITINATION2 (HUB2) in Arabidopsis. HUB2 has been previously...

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Autores principales: Zhang, Bo, Sztojka, Bernadette, Seyfferth, Carolin, Escamez, Sacha, Miskolczi, Pál, Chantreau, Maxime, Bakó, László, Delhomme, Nicolas, Gorzsás, András, Bhalerao, Rishikesh P, Tuominen, Hannele
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7501814/
https://www.ncbi.nlm.nih.gov/pubmed/32479638
http://dx.doi.org/10.1093/jxb/eraa264
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author Zhang, Bo
Sztojka, Bernadette
Seyfferth, Carolin
Escamez, Sacha
Miskolczi, Pál
Chantreau, Maxime
Bakó, László
Delhomme, Nicolas
Gorzsás, András
Bhalerao, Rishikesh P
Tuominen, Hannele
author_facet Zhang, Bo
Sztojka, Bernadette
Seyfferth, Carolin
Escamez, Sacha
Miskolczi, Pál
Chantreau, Maxime
Bakó, László
Delhomme, Nicolas
Gorzsás, András
Bhalerao, Rishikesh P
Tuominen, Hannele
author_sort Zhang, Bo
collection PubMed
description PIRIN2 (PRN2) was earlier reported to suppress syringyl (S)-type lignin accumulation of xylem vessels of Arabidopsis thaliana. In the present study, we report yeast two-hybrid results supporting the interaction of PRN2 with HISTONE MONOUBIQUITINATION2 (HUB2) in Arabidopsis. HUB2 has been previously implicated in several plant developmental processes, but not in lignification. Interaction between PRN2 and HUB2 was verified by β-galactosidase enzymatic and co-immunoprecipitation assays. HUB2 promoted the deposition of S-type lignin in the secondary cell walls of both stem and hypocotyl tissues, as analysed by pyrolysis-GC/MS. Chemical fingerprinting of individual xylem vessel cell walls by Raman and Fourier transform infrared microspectroscopy supported the function of HUB2 in lignin deposition. These results, together with a genetic analysis of the hub2 prn2 double mutant, support the antagonistic function of PRN2 and HUB2 in deposition of S-type lignin. Transcriptome analyses indicated the opposite regulation of the S-type lignin biosynthetic gene FERULATE-5-HYDROXYLASE1 by PRN2 and HUB2 as the underlying mechanism. PRN2 and HUB2 promoter activities co-localized in cells neighbouring the xylem vessel elements, suggesting that the S-type lignin-promoting function of HUB2 is antagonized by PRN2 for the benefit of the guaiacyl (G)-type lignin enrichment of the neighbouring xylem vessel elements.
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spelling pubmed-75018142020-09-23 The chromatin-modifying protein HUB2 is involved in the regulation of lignin composition in xylem vessels Zhang, Bo Sztojka, Bernadette Seyfferth, Carolin Escamez, Sacha Miskolczi, Pál Chantreau, Maxime Bakó, László Delhomme, Nicolas Gorzsás, András Bhalerao, Rishikesh P Tuominen, Hannele J Exp Bot Research Papers PIRIN2 (PRN2) was earlier reported to suppress syringyl (S)-type lignin accumulation of xylem vessels of Arabidopsis thaliana. In the present study, we report yeast two-hybrid results supporting the interaction of PRN2 with HISTONE MONOUBIQUITINATION2 (HUB2) in Arabidopsis. HUB2 has been previously implicated in several plant developmental processes, but not in lignification. Interaction between PRN2 and HUB2 was verified by β-galactosidase enzymatic and co-immunoprecipitation assays. HUB2 promoted the deposition of S-type lignin in the secondary cell walls of both stem and hypocotyl tissues, as analysed by pyrolysis-GC/MS. Chemical fingerprinting of individual xylem vessel cell walls by Raman and Fourier transform infrared microspectroscopy supported the function of HUB2 in lignin deposition. These results, together with a genetic analysis of the hub2 prn2 double mutant, support the antagonistic function of PRN2 and HUB2 in deposition of S-type lignin. Transcriptome analyses indicated the opposite regulation of the S-type lignin biosynthetic gene FERULATE-5-HYDROXYLASE1 by PRN2 and HUB2 as the underlying mechanism. PRN2 and HUB2 promoter activities co-localized in cells neighbouring the xylem vessel elements, suggesting that the S-type lignin-promoting function of HUB2 is antagonized by PRN2 for the benefit of the guaiacyl (G)-type lignin enrichment of the neighbouring xylem vessel elements. Oxford University Press 2020-06-01 /pmc/articles/PMC7501814/ /pubmed/32479638 http://dx.doi.org/10.1093/jxb/eraa264 Text en © The Author(s) 2020. Published by Oxford University Press on behalf of the Society for Experimental Biology. http://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Papers
Zhang, Bo
Sztojka, Bernadette
Seyfferth, Carolin
Escamez, Sacha
Miskolczi, Pál
Chantreau, Maxime
Bakó, László
Delhomme, Nicolas
Gorzsás, András
Bhalerao, Rishikesh P
Tuominen, Hannele
The chromatin-modifying protein HUB2 is involved in the regulation of lignin composition in xylem vessels
title The chromatin-modifying protein HUB2 is involved in the regulation of lignin composition in xylem vessels
title_full The chromatin-modifying protein HUB2 is involved in the regulation of lignin composition in xylem vessels
title_fullStr The chromatin-modifying protein HUB2 is involved in the regulation of lignin composition in xylem vessels
title_full_unstemmed The chromatin-modifying protein HUB2 is involved in the regulation of lignin composition in xylem vessels
title_short The chromatin-modifying protein HUB2 is involved in the regulation of lignin composition in xylem vessels
title_sort chromatin-modifying protein hub2 is involved in the regulation of lignin composition in xylem vessels
topic Research Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7501814/
https://www.ncbi.nlm.nih.gov/pubmed/32479638
http://dx.doi.org/10.1093/jxb/eraa264
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